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A polyalanine peptide derived from polar fish with anti-infectious activities

Due to the growing concern about antibiotic-resistant microbial infections, increasing support has been given to new drug discovery programs. A promising alternative to counter bacterial infections includes the antimicrobial peptides (AMPs), which have emerged as model molecules for rational design...

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Published in:Scientific reports 2016-02, Vol.6 (1), p.21385-21385, Article 21385
Main Authors: Cardoso, Marlon H., Ribeiro, Suzana M., Nolasco, Diego O., de la Fuente-Núñez, César, Felício, Mário R., Gonçalves, Sónia, Matos, Carolina O., Liao, Luciano M., Santos, Nuno C., Hancock, Robert E. W., Franco, Octávio L., Migliolo, Ludovico
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Language:English
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Summary:Due to the growing concern about antibiotic-resistant microbial infections, increasing support has been given to new drug discovery programs. A promising alternative to counter bacterial infections includes the antimicrobial peptides (AMPs), which have emerged as model molecules for rational design strategies. Here we focused on the study of Pa -MAP 1.9, a rationally designed AMP derived from the polar fish Pleuronectes americanus . Pa -MAP 1.9 was active against Gram-negative planktonic bacteria and biofilms, without being cytotoxic to mammalian cells. By using AFM, leakage assays, CD spectroscopy and in silico tools, we found that Pa -MAP 1.9 may be acting both on intracellular targets and on the bacterial surface, also being more efficient at interacting with anionic LUVs mimicking Gram-negative bacterial surface, where this peptide adopts α-helical conformations, than cholesterol-enriched LUVs mimicking mammalian cells. Thus, as bacteria present varied physiological features that favor antibiotic-resistance, Pa -MAP 1.9 could be a promising candidate in the development of tools against infections caused by pathogenic bacteria.
ISSN:2045-2322
2045-2322
DOI:10.1038/srep21385